6ehi
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NucT from Helicobacter pylori== | |
| + | <StructureSection load='6ehi' size='340' side='right'caption='[[6ehi]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ehi]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EHI FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ehi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ehi OCA], [https://pdbe.org/6ehi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ehi RCSB], [https://www.ebi.ac.uk/pdbsum/6ehi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ehi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A1V3AA65_HELPX A0A1V3AA65_HELPX] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Phospholipase D (PLD) superfamily of proteins includes a group of enzymes with nuclease activity on various nucleic acid substrates. Here, with the aim of better understanding the substrate specificity determinants in this subfamily, we have characterised the enzymatic activity and the crystal structure of NucT, a nuclease implicated in Helicobacter pylori purine salvage and natural transformation and compared them to those of its bacterial and mammalian homologues. NucT exhibits an endonuclease activity with a strong preference for single stranded nucleic acids substrates. We identified histidine124 as essential for the catalytic activity of the protein. Comparison of the NucT crystal structure at 1.58 A resolution reported here with those of other members of the sub-family suggests that the specificity of NucT for single-stranded nucleic acids is provided by the width of a positively charged groove giving access to the catalytic site. | ||
| - | + | Structural basis for the substrate selectivity of Helicobacter pylori NucT nuclease activity.,Celma L, Corbinais C, Vercruyssen J, Veaute X, de la Sierra-Gallay IL, Guerois R, Busso D, Mathieu A, Marsin S, Quevillon-Cheruel S, Radicella JP PLoS One. 2017 Dec 4;12(12):e0189049. doi: 10.1371/journal.pone.0189049., eCollection 2017. PMID:29206236<ref>PMID:29206236</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Li | + | <div class="pdbe-citations 6ehi" style="background-color:#fffaf0;"></div> |
| - | [[Category: Quevillon-Cheruel | + | == References == |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Helicobacter pylori]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Celma L]] | ||
| + | [[Category: Li de la Sierra-Gallay I]] | ||
| + | [[Category: Quevillon-Cheruel S]] | ||
Current revision
NucT from Helicobacter pylori
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